3fa4

X-ray diffraction
2.18Å resolution

Crystal structure of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member, triclinic crystal form

Released:

Function and Biology Details

Reaction catalysed:
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-173700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxaloacetate hydrolase class protein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 302 amino acids
Theoretical weight: 32.02 KDa
Source organism: Aspergillus niger
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2L887 (Residues: 2-303; Coverage: 100%)
Gene names: An07g08390, AnigIFM63604_010932, CAN33_0017865
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 79.09Å b: 115.47Å c: 115.75Å
α: 119.66° β: 90.71° γ: 96.28°
R-values:
R R work R free
0.204 0.2 0.265
Expression system: Escherichia coli